ID   SMC_DELAS               Reviewed;        1175 AA.
AC   A9BZW2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Daci_3590;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC       each terminus and a third globular domain forming a flexible SMC hinge
CC       near the middle of the molecule. These domains are separated by coiled-
CC       coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01894}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX36224.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000884; ABX36224.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043781925.1; NC_010002.1.
DR   AlphaFoldDB; A9BZW2; -.
DR   SMR; A9BZW2; -.
DR   STRING; 398578.Daci_3590; -.
DR   PRIDE; A9BZW2; -.
DR   EnsemblBacteria; ABX36224; ABX36224; Daci_3590.
DR   KEGG; dac:Daci_3590; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01894; Smc_prok; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   InterPro; IPR011890; SMC_prok.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1175
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409270"
FT   DOMAIN          524..625
FT                   /note="SMC hinge"
FT   REGION          807..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..504
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          684..918
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          944..1022
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COMPBIAS        828..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1175 AA;  131260 MW;  8E03C4D3CECA8C5C CRC64;
     MRLNSIKLSG FKSFAEPTNF MLPGQLVGVV GPNGCGKSNI MDAVRWVLGE SKASELRGES
     MQDVIFNGTT HRKPASRSSV ELVFDNSDHR AGGQWGQFGE IAVKRVLTRE GNSSYFINNQ
     AVRRRDVQDV FLGTGLGPRA YAIIGQGTIS RIIESRPEEL RLFLEEAAGV SKYKERRRET
     ENRLSATTEN LTRVEDILRE LNNNLDRLEK QAEVAAQYNA LQSQVTLKQQ QLWFLKRAEA
     EAEQDRVRVE GLQAVNELEE RMADIRNNES GLETLRQAHY DASDQVNQAQ AKLYESTAEV
     GKLEAEIRYV LEGRQRVQQR LQQLSEQVLL WNSRREEAEA EIENLEGAGM DAEEQAEMLA
     AQVEEQSMRL PDLEDALRNA QKADTDQRAS VVQVQQQIQV LAAEQRSLDE QRRQFETRFE
     RLRADRNALE TPDEARLNNL QSQLQEAREL AEMADAVLNE LQDSVPQLDE DRRTRQQAVN
     AEAARHADLS ARLEALKALQ EKVKTDGKLQ PWLAKHGLDG MQGLWSRIAI EPGWENALEA
     ALRERLGALE VGRLDMVRGF LGSGGHDAPP ARLAFFSPPQ GAPAPAAGRW QHLSDLLRVN
     DAGLRAVLGD WLQDCYTAPT LEEALSRRSE LRPGETVYVP TGHAVSSHSV SFYAQDSEQS
     GLLARAQEIE HLEKEVRAQA LISDESRTAL VRAESAYAEA SQRLVSARRE ASESQSRAHE
     LQVETLRLSQ LAEQARARNA QISADLAEVE AQLSDIEERR VAAEARFEEL DMQLADSQER
     HAQLGDKVLE SERRLNESRE QLRTLERQAQ EATFSRRSLE ARRGELSRTI ETASQQARSL
     ADEQQRAQDE LTRLTDAAAQ GGLQDALDLK MQREQAVAAR RSEYDDLTNK LRASDERRQQ
     LEKALDPLRQ RITEFQLKEQ AARLGLEQYS TLLEEAGADL AAVSQSIAEA NVRMHGLQGE
     IDRLHREIAA LGAVNLAALD ELKLARERKT FLDAQTEDLT QAMNTLEDAI RKIDAETREL
     LSGTFETVNG HFGRMFPELF GGGQAKLVIT GDEILDSGVQ VIAQPPGKKN QTIHLLSGGE
     KALTAIALVF AIFQLNPAPF CLLDEVDAPL DDANTERYAK LVASMSKSTQ FLFISHNKIA
     MEMAQQLIGV TMQEQGVSRI VAVDMESALS MAELS